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• W1784351639 abstract "The actin filament has clear polarity where one end, the pointed end, has a much slower polymerization and depolymerization rate than the other end, the barbed end. This intrinsic difference of the ends significantly affects all actin dynamics in the cell, which has central roles in a wide spectrum of cellular functions. The detailed mechanism underlying this difference has remained elusive, because high-resolution structures of the filament ends have not been available. Here, we present the structure of the actin filament pointed end obtained using a single particle analysis of cryo-electron micrographs. We determined that the terminal pointed end subunit is tilted towards the penultimate subunit, allowing specific and extra loop-to-loop inter-strand contacts between the two end subunits, which is not possible in other parts of the filament. These specific contacts prevent the end subunit from dissociating. For elongation, the loop-to-loop contacts also inhibit the incorporation of another actin monomer at the pointed end. These observations are likely to account for the less dynamic pointed end." @default.
• W1784351639 created "2016-06-24" @default.
• W1784351639 creator A5025325506 @default.
• W1784351639 creator A5057984567 @default.
• W1784351639 creator A5058058056 @default.
• W1784351639 date "2011-03-04" @default.
• W1784351639 modified "2023-10-18" @default.
• W1784351639 title "Structural basis for the slow dynamics of the actin filament pointed end" @default.
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• W1784351639 doi "https://doi.org/10.1038/emboj.2011.48" @default.
• W1784351639 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3094112" @default.
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